AU2003269225C1 - Humanized anti-granulocyte MN-3 antibody and uses thereof - Google Patents
Humanized anti-granulocyte MN-3 antibody and uses thereof Download PDFInfo
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- AU2003269225C1 AU2003269225C1 AU2003269225A AU2003269225A AU2003269225C1 AU 2003269225 C1 AU2003269225 C1 AU 2003269225C1 AU 2003269225 A AU2003269225 A AU 2003269225A AU 2003269225 A AU2003269225 A AU 2003269225A AU 2003269225 C1 AU2003269225 C1 AU 2003269225C1
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Classifications
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- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
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- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
- G01N33/574—Immunoassay; Biospecific binding assay; Materials therefor for cancer
- G01N33/57407—Specifically defined cancers
- G01N33/57426—Specifically defined cancers leukemia
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- A61K31/185—Acids; Anhydrides, halides or salts thereof, e.g. sulfur acids, imidic, hydrazonic or hydroximic acids
- A61K31/19—Carboxylic acids, e.g. valproic acid
- A61K31/20—Carboxylic acids, e.g. valproic acid having a carboxyl group bound to a chain of seven or more carbon atoms, e.g. stearic, palmitic, arachidic acids
- A61K31/203—Retinoic acids ; Salts thereof
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- A61K39/395—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum
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- A61K51/00—Preparations containing radioactive substances for use in therapy or testing in vivo
- A61K51/02—Preparations containing radioactive substances for use in therapy or testing in vivo characterised by the carrier, i.e. characterised by the agent or material covalently linked or complexing the radioactive nucleus
- A61K51/04—Organic compounds
- A61K51/08—Peptides, e.g. proteins, carriers being peptides, polyamino acids, proteins
- A61K51/10—Antibodies or immunoglobulins; Fragments thereof, the carrier being an antibody, an immunoglobulin or a fragment thereof, e.g. a camelised human single domain antibody or the Fc fragment of an antibody
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- A61K51/04—Organic compounds
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- A61K51/10—Antibodies or immunoglobulins; Fragments thereof, the carrier being an antibody, an immunoglobulin or a fragment thereof, e.g. a camelised human single domain antibody or the Fc fragment of an antibody
- A61K51/1027—Antibodies or immunoglobulins; Fragments thereof, the carrier being an antibody, an immunoglobulin or a fragment thereof, e.g. a camelised human single domain antibody or the Fc fragment of an antibody against receptors, cell-surface antigens or cell-surface determinants
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- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
- C07K16/2803—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against the immunoglobulin superfamily
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
- C07K2317/24—Immunoglobulins specific features characterized by taxonomic origin containing regions, domains or residues from different species, e.g. chimeric, humanized or veneered
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/56—Immunoglobulins specific features characterized by immunoglobulin fragments variable (Fv) region, i.e. VH and/or VL
- C07K2317/567—Framework region [FR]
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
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- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
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Landscapes
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- Chemical & Material Sciences (AREA)
- Immunology (AREA)
- Medicinal Chemistry (AREA)
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- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US41434102P | 2002-09-30 | 2002-09-30 | |
| US60/414,341 | 2002-09-30 | ||
| PCT/GB2003/004229 WO2004029093A2 (fr) | 2002-09-30 | 2003-09-30 | Anticorps anti-granulocytes chimeres, humains et humainises |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| AU2003269225A1 AU2003269225A1 (en) | 2004-04-19 |
| AU2003269225B2 AU2003269225B2 (en) | 2009-02-19 |
| AU2003269225C1 true AU2003269225C1 (en) | 2009-07-23 |
Family
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Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| AU2003269225A Ceased AU2003269225C1 (en) | 2002-09-30 | 2003-09-30 | Humanized anti-granulocyte MN-3 antibody and uses thereof |
Country Status (7)
| Country | Link |
|---|---|
| US (2) | US7541440B2 (fr) |
| EP (2) | EP2345673A1 (fr) |
| KR (1) | KR20050059220A (fr) |
| AU (1) | AU2003269225C1 (fr) |
| CA (1) | CA2500250C (fr) |
| IL (1) | IL167587A (fr) |
| WO (1) | WO2004029093A2 (fr) |
Families Citing this family (109)
| Publication number | Priority date | Publication date | Assignee | Title |
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| US7666400B2 (en) | 2005-04-06 | 2010-02-23 | Ibc Pharmaceuticals, Inc. | PEGylation by the dock and lock (DNL) technique |
| US7550143B2 (en) * | 2005-04-06 | 2009-06-23 | Ibc Pharmaceuticals, Inc. | Methods for generating stably linked complexes composed of homodimers, homotetramers or dimers of dimers and uses |
| US7981420B2 (en) | 2000-12-22 | 2011-07-19 | Max-Planck-Gesellschaft Zur Foederung Der Wissenschaften E.V. | Therapeutic use of antibodies directed against repulsive guidance molecule (RGM) |
| US8658773B2 (en) | 2011-05-02 | 2014-02-25 | Immunomedics, Inc. | Ultrafiltration concentration of allotype selected antibodies for small-volume administration |
| US20160279239A1 (en) | 2011-05-02 | 2016-09-29 | Immunomedics, Inc. | Subcutaneous administration of anti-cd74 antibody for systemic lupus erythematosus and autoimmune disease |
| US7906118B2 (en) | 2005-04-06 | 2011-03-15 | Ibc Pharmaceuticals, Inc. | Modular method to prepare tetrameric cytokines with improved pharmacokinetics by the dock-and-lock (DNL) technology |
| DE10303974A1 (de) | 2003-01-31 | 2004-08-05 | Abbott Gmbh & Co. Kg | Amyloid-β(1-42)-Oligomere, Verfahren zu deren Herstellung und deren Verwendung |
| JP4937751B2 (ja) * | 2003-06-13 | 2012-05-23 | イミューノメディクス、インコーポレイテッド | Ｄ−アミノ酸ペプチド |
| ES2432112T3 (es) * | 2004-02-10 | 2013-11-29 | The Regents Of The University Of Colorado, A Body Corporate | Inhibición del factor B, de la vía alternativa del complemento y métodos relacionados |
| US8034352B2 (en) * | 2005-04-06 | 2011-10-11 | Ibc Pharmaceuticals, Inc. | Tetrameric cytokines with improved biological activity |
| US8003111B2 (en) * | 2005-04-06 | 2011-08-23 | Ibc Pharmaceuticals, Inc. | Dimeric alpha interferon pegylated site-specifically shows enhanced and prolonged efficacy in vivo |
| US20110064754A1 (en) * | 2005-03-03 | 2011-03-17 | Center For Molecular Medicine And Immunology | Immunoconjugates Comprising Poxvirus-Derived Peptides and Antibodies Against Antigen-Presenting Cells for Subunit-Based Poxvirus Vaccines |
| US8652484B2 (en) | 2004-02-13 | 2014-02-18 | Immunomedics, Inc. | Delivery system for cytotoxic drugs by bispecific antibody pretargeting |
| US8551480B2 (en) | 2004-02-13 | 2013-10-08 | Immunomedics, Inc. | Compositions and methods of use of immunotoxins comprising ranpirnase (Rap) show potent cytotoxic activity |
| US8435539B2 (en) * | 2004-02-13 | 2013-05-07 | Immunomedics, Inc. | Delivery system for cytotoxic drugs by bispecific antibody pretargeting |
| US8491914B2 (en) | 2004-02-13 | 2013-07-23 | Ibc Pharmaceuticals, Inc. | Dock-and-lock (DNL) complexes for delivery of interference RNA |
| US20110020273A1 (en) * | 2005-04-06 | 2011-01-27 | Ibc Pharmaceuticals, Inc. | Bispecific Immunocytokine Dock-and-Lock (DNL) Complexes and Therapeutic Use Thereof |
| US7901680B2 (en) * | 2005-10-19 | 2011-03-08 | Ibc Pharmaceuticals, Inc. | Dock-and-lock (DNL) vaccines for cancer therapy |
| US9481878B2 (en) | 2004-02-13 | 2016-11-01 | Immunomedics, Inc. | Compositions and methods of use of immunotoxins comprising ranpirnase (Rap) show potent cytotoxic activity |
| US8562988B2 (en) * | 2005-10-19 | 2013-10-22 | Ibc Pharmaceuticals, Inc. | Strategies for improved cancer vaccines |
| ES2429541T3 (es) | 2004-11-16 | 2013-11-15 | Kalobios Pharmaceuticals, Inc. | Intercambio de casete de región variable de inmunoglobulina |
| AU2005313971B2 (en) * | 2004-12-08 | 2011-10-13 | Immunomedics, Inc. | Methods and compositions for immunotherapy and detection of inflammatory and immune-dysregulatory disease, infectious disease, pathologic angiogenesis and cancer |
| US20160355591A1 (en) | 2011-05-02 | 2016-12-08 | Immunomedics, Inc. | Subcutaneous anti-hla-dr monoclonal antibody for treatment of hematologic malignancies |
| US8481041B2 (en) | 2005-04-06 | 2013-07-09 | Ibc Pharmaceuticals, Inc. | Dock-and-lock (DNL) constructs for human immunodeficiency virus (HIV) therapy |
| US8067006B2 (en) | 2005-04-06 | 2011-11-29 | Immunomedics, Inc. | Polymeric carriers of therapeutic agents and recognition moieties for antibody-based targeting of disease sites |
| US8349332B2 (en) | 2005-04-06 | 2013-01-08 | Ibc Pharmaceuticals, Inc. | Multiple signaling pathways induced by hexavalent, monospecific and bispecific antibodies for enhanced toxicity to B-cell lymphomas and other diseases |
| US9623115B2 (en) | 2005-04-06 | 2017-04-18 | Ibc Pharmaceuticals, Inc. | Dock-and-Lock (DNL) Complexes for Disease Therapy |
| US9931413B2 (en) | 2005-04-06 | 2018-04-03 | Ibc Pharmaceuticals, Inc. | Tetrameric cytokines with improved biological activity |
| US8475794B2 (en) | 2005-04-06 | 2013-07-02 | Ibc Pharmaceuticals, Inc. | Combination therapy with anti-CD74 antibodies provides enhanced toxicity to malignancies, Autoimmune disease and other diseases |
| US8158129B2 (en) | 2005-04-06 | 2012-04-17 | Ibc Pharmaceuticals, Inc. | Dimeric alpha interferon PEGylated site-specifically shows enhanced and prolonged efficacy in vivo |
| US8911733B2 (en) * | 2005-05-26 | 2014-12-16 | Musc Foundation For Research Development | Inhibition of the alternative complement pathway for treatment of traumatic brain injury, spinal cord injury and related conditions |
| EP2594591B1 (fr) | 2005-08-11 | 2018-06-06 | Arpi Matossian-Rogers | Peptides associés au tcr-v beta pour traitement et diagnostic d'une maladie auto-immune |
| JP2009510002A (ja) | 2005-09-30 | 2009-03-12 | アボット ゲゼルシャフト ミット ベシュレンクテル ハフツング ウント コンパニー コマンディトゲゼルシャフト | 反発誘導分子（ｒｇｍ）タンパク質ファミリーのタンパク質の結合ドメイン、及びその機能的断片、及びそれらの使用 |
| EP1780220A1 (fr) * | 2005-11-01 | 2007-05-02 | Charité - Universitätsmedizin Berlin | Utilisation des substances de CEACAM8-specific pour traiter les maladies autoimmunes et une méthode pour examiner les substances qui induisent l'apoptosis |
| AU2006319361B2 (en) * | 2005-11-30 | 2011-09-22 | Therapharm Gmbh | Radioimmunoconjugate for human CD66 for the treatment of multiple myeloma |
| RU2442793C2 (ru) | 2005-11-30 | 2012-02-20 | Эбботт Лэборетриз | АНТИТЕЛА ПРОТИВ ГЛОБУЛОМЕРА Аβ, ИХ АНТИГЕНСВЯЗЫВАЮЩИЕ ЧАСТИ, СООТВЕТСТВУЮЩИЕ ГИБРИДОМЫ, НУКЛЕИНОВЫЕ КИСЛОТЫ, ВЕКТОРЫ, КЛЕТКИ-ХОЗЯЕВА, СПОСОБЫ ПОЛУЧЕНИЯ УКАЗАННЫХ АНТИТЕЛ, КОМПОЗИЦИИ, СОДЕРЖАЩИЕ УКАЗАННЫЕ АНТИТЕЛА, ПРИМЕНЕНИЯ УКАЗАННЫХ АНТИТЕЛ И СПОСОБЫ ИСПОЛЬЗОВАНИЯ УКАЗАННЫХ АНТИТЕЛ |
| SG2014013437A (en) | 2005-11-30 | 2014-07-30 | Abbott Lab | Monoclonal antibodies and uses thereof |
| KR100690199B1 (ko) * | 2006-04-20 | 2007-03-12 | 이화여자대학교 산학협력단 | 구리 이온 선택성을 갖는 플루오레세인 유도체, 이의제조방법 및 이를 이용한 생체 내 구리 이온 검출방법 |
| SI2409988T1 (sl) | 2006-06-13 | 2015-10-30 | Helix Biomedix Inc. | Peptidni fragmenti za sprožitev sinteze proteinov zunajcelične matrice |
| MX2009000476A (es) | 2006-07-14 | 2009-01-28 | Ac Immune Sa | Anticuerpo humanizado contra beta amiloide. |
| EP1914242A1 (fr) * | 2006-10-19 | 2008-04-23 | Sanofi-Aventis | Nouveau anticorps Anti-CD38 pour le traitement du cancer |
| US8455626B2 (en) | 2006-11-30 | 2013-06-04 | Abbott Laboratories | Aβ conformer selective anti-aβ globulomer monoclonal antibodies |
| WO2008085494A1 (fr) | 2007-01-05 | 2008-07-17 | Helix Biomedix Inc. | Peptides bioactifs pour modulation cellulaire et immunologique |
| CA2675014C (fr) * | 2007-01-17 | 2016-03-29 | Immunomedics, Inc. | Supports polymeres d'agents therapeutiques et fractions de reconnaissance pour un ciblage a base d'anticorps de sites de maladie |
| US20100311767A1 (en) | 2007-02-27 | 2010-12-09 | Abbott Gmbh & Co. Kg | Method for the treatment of amyloidoses |
| EP2236518B1 (fr) * | 2007-03-14 | 2014-08-06 | Alexion Cambridge Corporation | Anticorps humanisé contre le facteur B |
| US8048420B2 (en) | 2007-06-12 | 2011-11-01 | Ac Immune S.A. | Monoclonal antibody |
| US8613923B2 (en) | 2007-06-12 | 2013-12-24 | Ac Immune S.A. | Monoclonal antibody |
| EP2033971A1 (fr) * | 2007-09-06 | 2009-03-11 | Abbott GmbH & Co. KG | Domaines de protéines recombinantes des protéines morphogénétiques osseuses (BMP) de la famille des Repulsive Guidance Molecule (RGM) et leurs fragments fonctionnels ainsi que leur utilisation |
| WO2009048539A2 (fr) | 2007-10-05 | 2009-04-16 | Genentech, Inc. | Anticorps monoclonal |
| US8071555B2 (en) * | 2007-10-29 | 2011-12-06 | Helix Biomedix Inc. | Protective skin care peptides |
| US8557243B2 (en) | 2008-01-03 | 2013-10-15 | The Scripps Research Institute | EFGR antibodies comprising modular recognition domains |
| US8454960B2 (en) | 2008-01-03 | 2013-06-04 | The Scripps Research Institute | Multispecific antibody targeting and multivalency through modular recognition domains |
| US8557242B2 (en) | 2008-01-03 | 2013-10-15 | The Scripps Research Institute | ERBB2 antibodies comprising modular recognition domains |
| CN108864285A (zh) | 2008-01-03 | 2018-11-23 | 斯克里普斯研究院 | 通过模块识别结构域的抗体靶向 |
| US8574577B2 (en) | 2008-01-03 | 2013-11-05 | The Scripps Research Institute | VEGF antibodies comprising modular recognition domains |
| US8962803B2 (en) * | 2008-02-29 | 2015-02-24 | AbbVie Deutschland GmbH & Co. KG | Antibodies against the RGM A protein and uses thereof |
| US8623322B2 (en) | 2008-06-13 | 2014-01-07 | Stc.Unm | Non-invasive diagnostic agents and methods of diagnosing infectious disease |
| PL3903829T3 (pl) | 2009-02-13 | 2023-08-14 | Immunomedics, Inc. | Immunokoniugaty z połączeniem rozszczepialnym wewnątrzkomórkowo |
| US20160095939A1 (en) | 2014-10-07 | 2016-04-07 | Immunomedics, Inc. | Neoadjuvant use of antibody-drug conjugates |
| AU2010266127B2 (en) | 2009-07-02 | 2015-11-05 | Musc Foundation For Research Development | Methods of stimulating liver regeneration |
| IN2012DN00454A (fr) * | 2009-07-16 | 2015-05-15 | Beckman Coulter Inc | |
| CA2774260C (fr) * | 2009-09-16 | 2018-10-09 | Immunomedics, Inc. | Anticorps anti-cea de classe i et leurs utilisations |
| EP2506881B1 (fr) | 2009-12-02 | 2024-03-06 | Immunomedics, Inc. | Combinaison de radioimmunotherapie et conjugues anticorps-medicament pour une meilleure therapie du cancer |
| MX2012006560A (es) * | 2009-12-08 | 2012-10-05 | Abbott Gmbh & Co Kg | Anticuerpos monoclonales contra la proteina rgm a para utilizarse en el tratamiento de degeneracion de capa de fibra de nervio retinal. |
| MX360403B (es) | 2010-04-15 | 2018-10-31 | Abbvie Inc | Proteinas de union a amiloide beta. |
| WO2011144744A1 (fr) * | 2010-05-20 | 2011-11-24 | Therapharm Gmbh | Composé radioactif ciblé pour cd66 humain pour le traitement de troubles |
| WO2012009705A1 (fr) | 2010-07-15 | 2012-01-19 | Zyngenia, Inc. | Complexes liant ang-2 et leurs utilisations |
| KR101713365B1 (ko) | 2010-07-30 | 2017-03-08 | 에이씨 이뮨 에스.에이. | 안전하고 기능적인 인간화 항 베타-아밀로이드 항체 |
| JP6147665B2 (ja) | 2010-08-14 | 2017-06-14 | アッヴィ・インコーポレイテッド | アミロイドベータ結合タンパク質 |
| EP2643483A4 (fr) * | 2010-11-26 | 2014-04-30 | Immunexpress Pty Ltd | Agents de diagnostic et/ou de criblage et utilisations de ceux-ci |
| WO2012162561A2 (fr) | 2011-05-24 | 2012-11-29 | Zyngenia, Inc. | Complexes plurispécifiques multivalents et monovalents, et leurs utilisations |
| WO2012178151A2 (fr) * | 2011-06-24 | 2012-12-27 | Health Research, Inc. | Modulation de l'hématopoïèse induite par les st6gal 1 |
| PL2807192T3 (pl) | 2012-01-27 | 2019-02-28 | Abbvie Deutschland | Kompozycja oraz sposób diagnostyki i leczenia chorób związanych ze zwyrodnieniem neurytów |
| EP2855529A4 (fr) | 2012-05-24 | 2015-12-09 | Alexion Pharma Inc | Anticorps anti-facteur b humaneered |
| AU2013302696B9 (en) | 2012-08-14 | 2018-08-09 | Ibc Pharmaceuticals, Inc. | T-cell redirecting bispecific antibodies for treatment of disease |
| CN104837502B (zh) | 2012-10-12 | 2018-08-10 | 麦迪穆有限责任公司 | 吡咯并苯并二氮杂卓及其结合物 |
| BR112015013444B1 (pt) | 2012-12-13 | 2022-11-01 | Immunomedics, Inc | Uso de um imunoconjugado |
| AU2013204922B2 (en) | 2012-12-20 | 2015-05-14 | Celgene Corporation | Chimeric antigen receptors |
| EP2774930A1 (fr) | 2013-03-07 | 2014-09-10 | Aptenia S.R.L. | Composés de métallocène et molécules marquées comprenant ceux-ci pour l'imagerie in vivo |
| JP6444902B2 (ja) | 2013-03-13 | 2018-12-26 | メドイミューン・リミテッドＭｅｄＩｍｍｕｎｅ Ｌｉｍｉｔｅｄ | ピロロベンゾジアゼピン及びその結合体 |
| CA2907397C (fr) | 2013-03-15 | 2022-11-22 | Anthrogenesis Corporation | Lymphocytes t modifies |
| US10150800B2 (en) | 2013-03-15 | 2018-12-11 | Zyngenia, Inc. | EGFR-binding modular recognition domains |
| AU2015219495B2 (en) | 2014-02-21 | 2019-11-21 | Ibc Pharmaceuticals, Inc. | Disease therapy by inducing immune response to Trop-2 expressing cells |
| EP3110445A4 (fr) | 2014-02-25 | 2017-09-27 | Immunomedics, Inc. | Anticorps rfb4 humanisés anti-cd22 |
| SG11201608194VA (en) | 2014-04-03 | 2016-10-28 | Igm Biosciences Inc | Modified j-chain |
| US9580495B2 (en) | 2014-06-24 | 2017-02-28 | Immunomedics, Inc. | Anti-histone therapy for vascular necrosis in severe glomerulonephritis |
| JP7080055B2 (ja) | 2014-09-08 | 2022-06-03 | ルタナ ゲーエムベーハー | 細胞の細胞質への分子の送達のための構築物 |
| US10188746B2 (en) | 2014-09-10 | 2019-01-29 | Medimmune Limited | Pyrrolobenzodiazepines and conjugates thereof |
| EP3789039A1 (fr) * | 2014-12-22 | 2021-03-10 | The Rockefeller University | Anticorps agonistes anti-mertk et leurs utilisations |
| JP6746845B2 (ja) | 2015-04-22 | 2020-08-26 | イミューノメディクス、インコーポレイテッドＩｍｍｕｎｏｍｅｄｉｃｓ， Ｉｎｃ． | 循環ｔｒｏｐ−２陽性癌細胞の単離、検出、診断及び／または特徴付け |
| EP3313443B9 (fr) | 2015-06-25 | 2023-10-04 | Immunomedics, Inc. | Combinaison d'anticorps anti-hla-dr ou anti-trop-2 avec des inhibiteurs de microtubule, des inhibiteurs de parp, des inhibiteurs de kinase de bruton ou des inhibiteurs de phosphoinositide 3-kinase améliorant considérablement un résultat thérapeutique de cancer |
| EP3316885B1 (fr) | 2015-07-01 | 2021-06-23 | Immunomedics, Inc. | Immunoconjugués d'anticorps sn-38 avec un lieur cl2a |
| EP3356401B1 (fr) | 2015-09-30 | 2020-06-24 | IGM Biosciences, Inc. | Molécules de liaison à chaîne j modifiée |
| EP3355913A1 (fr) | 2015-09-30 | 2018-08-08 | IGM Biosciences A/S | Molécules de liaison à chaîne j modifiée |
| EP3525829A1 (fr) | 2016-10-11 | 2019-08-21 | Medimmune Limited | Conjugués anticorps-médicament associés à des agents thérapeutiques à médiation immunitaire |
| US11331380B2 (en) | 2016-10-20 | 2022-05-17 | Celgene Corporation | Cereblon-based heterodimerizable chimeric antigen receptors |
| US20190274645A1 (en) * | 2016-10-26 | 2019-09-12 | Cao Group, Inc. | Cancer binding radio-opaque peptides that are targeted for disintegration by radiant energy |
| US10799597B2 (en) | 2017-04-03 | 2020-10-13 | Immunomedics, Inc. | Subcutaneous administration of antibody-drug conjugates for cancer therapy |
| CN113286616A (zh) | 2018-05-23 | 2021-08-20 | Adc治疗有限公司 | 分子佐剂 |
| WO2020064847A1 (fr) | 2018-09-26 | 2020-04-02 | Ascendis Pharma A/S | Hydrogels dégradables d'acide hyaluronique |
| JP2022514615A (ja) | 2018-12-20 | 2022-02-14 | アルバート アインシュタイン カレッジ オブ メディスン | ヒト免疫チェックポイントＣＥＡＣＡＭ１（ＣＤ６６ａ）に対するアンタゴニスト抗体及びその製剤、キット並びに使用方法 |
| US20230137434A1 (en) * | 2020-03-19 | 2023-05-04 | Vascular Biosciences | CAR Peptide for Improved Coronavirus Survival |
| WO2022010797A2 (fr) | 2020-07-07 | 2022-01-13 | Bionecure Therapeutics, Inc. | Nouveaux maytansinoïdes en tant que charges utiles d'adc et leur utilisation pour le traitement du cancer |
| WO2022008699A1 (fr) | 2020-07-09 | 2022-01-13 | F. Hoffmann-La Roche Ag | Compositions concentrées de protéines, leur préparation et l'utilisation associée |
| GB202102396D0 (en) | 2021-02-19 | 2021-04-07 | Adc Therapeutics Sa | Molecular adjuvant |
| WO2022239720A1 (fr) | 2021-05-10 | 2022-11-17 | 公益財団法人川崎市産業振興財団 | Anticorps d'affinité de liaison vis-à-vis d'antigènes réduite |
| WO2023016488A1 (fr) | 2021-08-13 | 2023-02-16 | 昆山新蕴达生物科技有限公司 | Conjugué anticorps-médicament à base d'inhibiteur de microtubules |
| WO2023024949A1 (fr) | 2021-08-24 | 2023-03-02 | 昆山新蕴达生物科技有限公司 | Conjugué anticorps-médicament conjugué par l'intermédiaire d'un lieur cassable |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20020022031A1 (en) * | 2000-08-08 | 2002-02-21 | Goldenberg David M. | Immunotherapy for chronic myelocytic leukemia |
| AU2003244766A1 (en) * | 2002-06-07 | 2003-12-22 | Immunomedics, Inc. | Neutrophil imaging methods in cyctic fibrosis |
Family Cites Families (30)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4036945A (en) | 1976-05-03 | 1977-07-19 | The Massachusetts General Hospital | Composition and method for determining the size and location of myocardial infarcts |
| US4331647A (en) | 1980-03-03 | 1982-05-25 | Goldenberg Milton David | Tumor localization and therapy with labeled antibody fragments specific to tumor-associated markers |
| US4818709A (en) | 1983-01-21 | 1989-04-04 | Primus Frederick J | CEA-family antigens, Anti-CEA antibodies and CEA immunoassay |
| GB8308235D0 (en) * | 1983-03-25 | 1983-05-05 | Celltech Ltd | Polypeptides |
| US4816567A (en) * | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
| US5776093A (en) | 1985-07-05 | 1998-07-07 | Immunomedics, Inc. | Method for imaging and treating organs and tissues |
| US5618920A (en) * | 1985-11-01 | 1997-04-08 | Xoma Corporation | Modular assembly of antibody genes, antibodies prepared thereby and use |
| US5057313A (en) | 1986-02-25 | 1991-10-15 | The Center For Molecular Medicine And Immunology | Diagnostic and therapeutic antibody conjugates |
| US4946778A (en) | 1987-09-21 | 1990-08-07 | Genex Corporation | Single polypeptide chain binding molecules |
| US4704692A (en) | 1986-09-02 | 1987-11-03 | Ladner Robert C | Computer based system and method for determining and displaying possible chemical structures for converting double- or multiple-chain polypeptides to single-chain polypeptides |
| US5567610A (en) | 1986-09-04 | 1996-10-22 | Bioinvent International Ab | Method of producing human monoclonal antibodies and kit therefor |
| US5258498A (en) * | 1987-05-21 | 1993-11-02 | Creative Biomolecules, Inc. | Polypeptide linkers for production of biosynthetic proteins |
| KR0162259B1 (ko) * | 1989-12-05 | 1998-12-01 | 아미 펙터 | 감염성 병변 및 염증성 병변을 검출 및 치료하기 위한 키메라 항체 |
| US5229275A (en) | 1990-04-26 | 1993-07-20 | Akzo N.V. | In-vitro method for producing antigen-specific human monoclonal antibodies |
| US5633425A (en) | 1990-08-29 | 1997-05-27 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| US5994510A (en) * | 1990-12-21 | 1999-11-30 | Celltech Therapeutics Limited | Recombinant antibodies specific for TNFα |
| US6096289A (en) | 1992-05-06 | 2000-08-01 | Immunomedics, Inc. | Intraoperative, intravascular, and endoscopic tumor and lesion detection, biopsy and therapy |
| CA2133580A1 (fr) | 1992-05-06 | 1993-11-11 | David M. Goldenberg | Detection et traitement des tumeurs et des lesions par voies peroperatoire, intravasculaire et endoscopique |
| US5443953A (en) | 1993-12-08 | 1995-08-22 | Immunomedics, Inc. | Preparation and use of immunoconjugates |
| US5827690A (en) | 1993-12-20 | 1998-10-27 | Genzyme Transgenics Corporatiion | Transgenic production of antibodies in milk |
| AUPO591797A0 (en) | 1997-03-27 | 1997-04-24 | Commonwealth Scientific And Industrial Research Organisation | High avidity polyvalent and polyspecific reagents |
| US5753206A (en) | 1995-06-07 | 1998-05-19 | Immunomedics, Inc. | Radiometal-binding analogues of luteinizing hormone releasing hormone |
| CA2249320C (fr) | 1996-03-20 | 2008-12-23 | Immunomedics, Inc. | Anticorps humanises glycosyles specifiques des lymphocytes b |
| DE69737867T2 (de) | 1996-05-03 | 2007-10-18 | Immunomedics, Inc. | Zielgerichtete kombinations-immuntherapie für krebs |
| US6962702B2 (en) * | 1998-06-22 | 2005-11-08 | Immunomedics Inc. | Production and use of novel peptide-based agents for use with bi-specific antibodies |
| ATE384792T1 (de) | 1998-11-18 | 2008-02-15 | Genentech Inc | Antikörpervarianten mit höheren bindungsaffinitäten im vergleich zu parentalen antikörpern |
| DE60043273D1 (de) | 1999-04-15 | 2009-12-17 | Crucell Holland Bv | Verwendung von Rekombinanten Proteinen in Menschlichen Zellen |
| JP2001299349A (ja) * | 2000-04-19 | 2001-10-30 | Suntory Ltd | 新規組換え型抗体とそのｃｄｒのアミノ酸配列およびそれをコードする遺伝子 |
| US7390885B2 (en) * | 2001-11-26 | 2008-06-24 | Cell Matrix, Inc. | Humanized collagen antibodies and related methods |
| US7538195B2 (en) * | 2002-06-14 | 2009-05-26 | Immunogen Inc. | Anti-IGF-I receptor antibody |
-
2003
- 2003-09-29 US US10/672,278 patent/US7541440B2/en not_active Expired - Fee Related
- 2003-09-30 EP EP20100012293 patent/EP2345673A1/fr not_active Ceased
- 2003-09-30 CA CA2500250A patent/CA2500250C/fr not_active Expired - Fee Related
- 2003-09-30 EP EP03751001.3A patent/EP1546204B1/fr not_active Expired - Lifetime
- 2003-09-30 WO PCT/GB2003/004229 patent/WO2004029093A2/fr not_active Application Discontinuation
- 2003-09-30 KR KR1020057005541A patent/KR20050059220A/ko not_active Application Discontinuation
- 2003-09-30 AU AU2003269225A patent/AU2003269225C1/en not_active Ceased
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2005
- 2005-03-22 IL IL167587A patent/IL167587A/en active IP Right Grant
-
2009
- 2009-03-05 US US12/398,416 patent/US7951369B2/en not_active Expired - Fee Related
Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20020022031A1 (en) * | 2000-08-08 | 2002-02-21 | Goldenberg David M. | Immunotherapy for chronic myelocytic leukemia |
| AU2003244766A1 (en) * | 2002-06-07 | 2003-12-22 | Immunomedics, Inc. | Neutrophil imaging methods in cyctic fibrosis |
Also Published As
| Publication number | Publication date |
|---|---|
| AU2003269225B2 (en) | 2009-02-19 |
| CA2500250A1 (fr) | 2004-04-08 |
| AU2003269225A1 (en) | 2004-04-19 |
| EP2345673A1 (fr) | 2011-07-20 |
| EP1546204A2 (fr) | 2005-06-29 |
| EP1546204B1 (fr) | 2013-09-18 |
| US20090185974A1 (en) | 2009-07-23 |
| US20070183970A1 (en) | 2007-08-09 |
| IL167587A (en) | 2011-04-28 |
| US7951369B2 (en) | 2011-05-31 |
| WO2004029093A2 (fr) | 2004-04-08 |
| CA2500250C (fr) | 2015-11-24 |
| WO2004029093A3 (fr) | 2004-06-03 |
| US7541440B2 (en) | 2009-06-02 |
| KR20050059220A (ko) | 2005-06-17 |
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